EP1449921A2 - Nouveaux polypeptides biologiquement actifs, leur préparation et composition pharmaceutique les contenant - Google Patents
Nouveaux polypeptides biologiquement actifs, leur préparation et composition pharmaceutique les contenant Download PDFInfo
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- EP1449921A2 EP1449921A2 EP04075986A EP04075986A EP1449921A2 EP 1449921 A2 EP1449921 A2 EP 1449921A2 EP 04075986 A EP04075986 A EP 04075986A EP 04075986 A EP04075986 A EP 04075986A EP 1449921 A2 EP1449921 A2 EP 1449921A2
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- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/02—Fusion polypeptide containing a localisation/targetting motif containing a signal sequence
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/31—Fusion polypeptide fusions, other than Fc, for prolonged plasma life, e.g. albumin
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/33—Fusion polypeptide fusions for targeting to specific cell types, e.g. tissue specific targeting, targeting of a bacterial subspecies
Definitions
- the present invention relates to polypeptides recombinants essentially composed of an active part derived from a polypeptide, natural or artificial, having therapeutic activity, and coupled with albumin or a variant of albumin. It is understood that the therapeutic activity of the polypeptides of the invention can be either direct (treatment of diseases), or indirect (and by example usable in disease prevention, in vaccine design, in medical imaging techniques etc ).
- the aim of the present invention is to develop biologically active artificial proteins which can be used from the pharmaceutical point of view. Indeed, many polypeptides having one or more potential therapeutic activities cannot be exploited pharmaceutically. This can have different reasons, such as in particular their low stability in vivo , their complex or fragile structure, the difficulty of producing them on an industrially acceptable scale, etc. Similarly, certain polypeptides do not give the expected results in vivo in due to problems with administration, packaging, pharmacokinetics, etc.
- the present invention overcomes these drawbacks.
- the current invention indeed provides new molecules allowing exploitation optimal therapeutically biological properties of these polypeptides.
- the present invention results in particular from the demonstration that it is possible to genetically coupling any active structure derived from a polypeptide biologically active to another protein structure consisting of albumin, without alter said biological properties. It also results from the highlighting by the applicant that human serum albumin makes it possible to present effectively the active structure at its interaction sites, and that it ensures stability high plasma level of the inventive polypeptide.
- the polypeptides of the invention thus allow to maintain in the organism a given biological activity for an extended time. They thus make it possible to reduce the doses administered and, in some cases, to potentiate the therapeutic effect, for example by reducing side effects following increased administration.
- polypeptides of the invention also make it possible to generate and use structures derived from biologically active polypeptides very small and therefore very specific for an effect research. It is understood that the peptides having a biological activity exhibiting a therapeutic interest can also correspond to peptide sequences non-natural, isolated for example from random peptide banks.
- the polypeptides of the invention moreover have a particularly beneficial in the body, which changes their pharmacokinetic properties and promotes the development of their biological activity and their use. In addition, they also have the advantage of being weakly or non-immunogenic for the organism in which they are used.
- the polypeptides of the invention can be expressed (and preferably secreted) by organisms recombinant, at levels allowing their industrial exploitation.
- An object of the present invention therefore relates to polypeptides comprising an active part derived from a polypeptide having an activity therapeutic, coupled with albumin or a variant of albumin.
- the polypeptide having therapeutic activity is a polypeptide of human origin or a variant molecular.
- it may be all or part, an enzyme, a enzyme, antigen, antibody, hormone, factor inhibitor involved in the control of coagulation, an interferon, a cytokine [the interleukins, but also their natural antagonistic variants of their attachment to (x) receptor (s), SIS (small induced secreted) type cytokines and for example macrophage inflammatory proteins (MIPs), etc ...], a factor of growth and / or differentiation [and for example growth factors transformants (TGFs), differentiating factors of blood cells (erythropoietin, M-CSF, G-CSF, GM-CSF etc.), insulin and the growth that resemble it (IGFs), or the permeability factors cell (VPF / VEGF), etc.], of a factor involved in the genesis / resorption of bone tissue (OIF and osteospontine for
- the active part of the molecules of the invention can be coupled either directly either through an artificial albumin peptide.
- she can constitute the N-terminal end as the C-terminal end of the molecule.
- the active part constitutes the C-terminal part of the chimera. It is also understood that the part biologically active may be redundant within the chimera.
- a representation schematic of the molecules of the invention is given in Figure 1.
- expression plasmids can be shuttle vectors between a bacterial host such as Escherichia coli and the selected host cell.
- a bacterial host such as Escherichia coli
- an origin of replication and a selection marker functioning in the bacterial host are required.
- any method which makes it possible to introduce foreign DNA into a cell can be used. It may especially be transformation, electroporation, conjugation, or any other technique known to those skilled in the art.
- the different Kluyveromyces strains used were transformed by treating the whole cells in the presence of lithium acetate and polyethylene glycol, according to the technique described by Ito et al. [J. Bacteriol. 153 (1983) 163].
- the transformation technique described by Durrens et al. [Curr. Broom. 18 (1990) 7] using ethylene glycol and dimethyl sulfoxide was also used. It is also possible to transform yeasts by electroporation, according to the method described by Karube et al. [FEBS Letters 182 (1985) 90].
- An alternative protocol is also described in detail in the examples which follow.
- the present invention also relates to the nucleotide sequences encoding the chimeric polypeptides described above, as well as the cells recombinant, eukaryotic or prokaryotic, comprising such sequences.
- the protruding 5 'ends are filled with the Klenow fragment of DNA polymerase I from E. coli (Biolabs) according to the supplier's specifications.
- the destruction of the prominent 3 'ends is carried out in the presence of the DNA Polymerase of phage T4 (Biolabs) used according to the manufacturer's recommendations.
- the destruction of the protruding 5 ′ ends is carried out by gentle treatment with nuclease S1.
- Transformations of K. lactis with the DNA of the protein expression plasmids of the present invention are carried out by any technique known to a person skilled in the art, an example of which is given in the text.
- the bacterial strains used are E. coli MC1060 ( lac IPOZYA, X74, gal U, gal K, Str A r ), or E. coli TG1 ( lac , pro A, B, sup E, thi , hsd D5 / F tra D36, pro A + B + , lake I q , lake Z, M15).
- hybrid genes coding for a chimeric protein resulting from the translational coupling between the mature form of HSA, or one of its molecular variants, and a biologically active peptide coupled to the N- and C-terminal ends of HSA.
- These hybrid genes are preferably bordered 5 'to the translation initiating ATG and 3' to the translation end codon by Hind III restriction sites and encode chimeric proteins of the PEPTIDE-SAH-PEPTIDE type (FIG. 1, panel C), immediately preceded by the SAH "prepro" export region.
- the biologically active peptide can be present more than once in the chimera.
- the transformation of yeasts belonging to the genus Kluyveromyces, and in particular the strains MW98-8C and CBS 293.91 of K. lactis, is carried out for example by the technique of treatment of whole cells with lithium acetate [Ito H. et al., J. Bacteriol. 153 (1983) 163-168], adapted as follows.
- the vWF binding site is a peptide including residues Thr470 to Asp498 of mature vWF.
- This sequence includes the peptide G10 (Cys474-Pro488) described by Mori et al. [J. Biol. Chem. 263 (1988) 17901-17904] and capable of antagonizing the interaction of human vWF with GP1b of human platelets.
- the sequence corresponding to the G10 peptide is first included in an Mst II- Hind III restriction fragment (FIG.
Abstract
Description
Claims (19)
- Polypeptide recombinant comportant une partie active dérivée d'un polypeptide ayant une activité thérapeutique, génétiquement couplée à une albumine ou à un variant de l'albumine.
- Polypeptide selon la revendication 1 caractérisé en ce que le polypeptide ayant une activité thérapeutique est un polypeptide d'origine humaine.
- Polypeptide selon la revendication 2 caractérisé en ce que le polypeptide ayant une activité thérapeutique est choisi parmi tout ou partie des enzymes, des inhibiteurs d'enzymes, des antigènes, des anticorps, des hormones, des facteurs de la coagulation, des interférons, des cytokines, des facteurs de croissance et/ou de différenciation, des facteurs impliqués dans la génèse/résorption des tissus osseux, des facteurs chimiotactiques, des facteurs de motilité ou de migration cellulaire, des facteurs cytostatiques, des facteurs bactéricides ou antifongiques, ou des molécules adhésives plasmatiques, interstitielles ou des matrices extracellulaires.
- Polypeptide selon l'une des revendications 1 à 3 caractérisé en ce que le polypeptide ayant une activité thérapeutique est choisi parmi toute séquence peptidique antagoniste ou agoniste d'interactions moléculaires et/ou cellulaires impliquées dans les pathologies des compartiments circulatoires et interstitiels.
- Polypeptide selon l'une des revendications 1 à 4 caractérisé en ce que la partie active présente une structure choisie parmi :(a) la structure peptidique entière ou,(b) un fragment de (a) ou une structure dérivée de (a) par modification structurale (mutation, substitution addition et/ou délétion d'un ou plusieurs résidus) et conservant une activité thérapeutique.
- Polypeptide selon l'une des revendications 1 à 5 caractérisé en ce que la partie active est couplée à l'extrémité N-terminale de l'albumine.
- Polypeptide selon l'une des revendications 1 à 5 caractérisé en ce que la partie active est couplée à l'extrémité C-terminale de l'albumine.
- Polypeptide selon l'une des revendications 1 à 7 caractérisé en ce que la partie active y est représenté plusieurs fois.
- Séquence nucléotidique codant pour un polypeptide selon l'une quelconque des revendications 1 à 8.
- Séquence nucléotidique selon la revendication 9 caractérisée en ce qu'elle comprend une séquence "leader" permettant la sécrétion du polypeptide exprimé.
- Cassette d'expression comprenant une séquence nucléotidique selon l'une des revendications 9 ou 10 sous le contrôle d'une région d'initiation de la transcription et éventuellement d'une région de terminaison de la transcription.
- Plasmide autoréplicatif comportant une cassette d'expression selon la revendication 11.
- Cellule recombinante eucaryote ou procaryote dans laquelle a été inséré une séquence nucléotidique selon l'une des revendications 9 ou 10 ou une cassette d'expression selon la revendication 11 ou un plasmide selon la revendication 12.
- Cellule recombinante selon la revendication 13 caractérisée en ce qu'il s'agit d'une levure, d'une cellule animale, d'un champignon ou d'une bactérie.
- Cellule recombinante selon la revendication 14 caractérisée en ce qu'il s'agit d'une levure.
- Cellule recombinante selon la revendication 15 caractérisée en ce qu'il s'agit d'une levure du genre Saccharomyces ou Kluyveromyces.
- Procédé de préparation d'un polypeptide tel que défini dans l'une des revendications 1 à 8 caractérisé en ce que l'on cultive une cellule recombinante selon l'une des revendications 13 à 16 dans des conditions d'expression, et on récupère le polypeptide produit.
- Composition pharmaceutique comprenant un ou plusieurs polypeptides selon l'une quelconque des revendications 1 à 8.
- Composition pharmaceutique comprenant une séquence nucléotidique selon l'une quelconque des revendications 9 à 11 utilisable en thérapie génique.
Applications Claiming Priority (3)
Application Number | Priority Date | Filing Date | Title |
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FR9201064A FR2686899B1 (fr) | 1992-01-31 | 1992-01-31 | Nouveaux polypeptides biologiquement actifs, leur preparation et compositions pharmaceutiques les contenant. |
FR9201064 | 1992-01-31 | ||
EP93904129A EP0624195B1 (fr) | 1992-01-31 | 1993-01-28 | Nouveaux polypeptides biologiquement actifs, leur preparation et composition pharmaceutique les contenant |
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EP93904129A Division EP0624195B1 (fr) | 1992-01-31 | 1993-01-28 | Nouveaux polypeptides biologiquement actifs, leur preparation et composition pharmaceutique les contenant |
EP93904129.9 Division | 1993-08-08 |
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EP1449921A3 EP1449921A3 (fr) | 2006-01-11 |
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EP93904129A Expired - Lifetime EP0624195B1 (fr) | 1992-01-31 | 1993-01-28 | Nouveaux polypeptides biologiquement actifs, leur preparation et composition pharmaceutique les contenant |
EP04075986A Withdrawn EP1449921A3 (fr) | 1992-01-31 | 1993-01-28 | Nouveaux polypeptides biologiquement actifs, leur préparation et composition pharmaceutique les contenant |
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Country Status (13)
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US (12) | US5876969A (fr) |
EP (2) | EP0624195B1 (fr) |
JP (3) | JPH07503368A (fr) |
AT (1) | ATE276361T1 (fr) |
CA (1) | CA2126091C (fr) |
DE (1) | DE69333622T2 (fr) |
DK (1) | DK0624195T3 (fr) |
ES (1) | ES2230541T3 (fr) |
FI (1) | FI120355B (fr) |
FR (1) | FR2686899B1 (fr) |
NO (2) | NO325486B1 (fr) |
PT (1) | PT624195E (fr) |
WO (1) | WO1993015199A1 (fr) |
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